Related Experiment Videos
Tyr-571 is involved in the T7 RNA polymerase binding to its promoter
V O Rechinsky1, V L Tunitskaya, S M Dragan
1V.A. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.
FEBS Letters
|March 29, 1993
Abstract:
The in vitro studies of three T7 RNA polymerase point mutants suggest that substitutions of Ala and Thr for Pro-563 and of Ser for Tyr-571 have little effect on the enzyme catalytic competence, but result in its inability to utilize the promoter. Both P563A and P563T mutants retain the promoter-binding ability, whereas the promoter affinity of the Y571S mutant drops drastically.